Catalase-peroxidase - Rhizobium radiobacter (Agrobacterium tumefaciens)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Catalase-peroxidase
Short name=CP
EC=1.11.1.21

Alternative name(s):
Peroxidase/catalase

Gene names

Name:	katG
Synonyms:	katA

Organism

Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)

Taxonomic identifier

358 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. Involved in tumorigenesis. Ref.1
Catalytic activity	Donor + H₂O₂ = oxidized donor + 2 H₂O. HAMAP MF_01961 2 H₂O₂ = O₂ + 2 H₂O. HAMAP MF_01961
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity.
Subunit structure	Homodimer or homotetramer By similarity. HAMAP MF_01961
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 723

723

Catalase-peroxidase HAMAP MF_01961

PRO_0000354715

Sites

Active site

98

1

Proton acceptor By similarity

Metal binding

266

1

Iron (heme axial ligand) By similarity

Site

94

1

Transition state stabilizer By similarity

Amino acid modifications

Cross-link

97 ↔ 225

Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-251) By similarity

Cross-link

225 ↔ 251

Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-97) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9R708 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: AA531987F535B508
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FASTA

723

78,741

        10         20         30         40         50         60 
MDATSKPAGK CPVMHGGNTV SGKSVTEWWP NALNLDILHQ HDTKTNPLGT SFNYREALKT 

        70         80         90        100        110        120 
LDVEALKADL RALMTDSQEW WPADWGSYVG MMARVTWHAA GSYRVTDGRG GANTGNQRFA 

       130        140        150        160        170        180 
PLNSWPDNVN TDKGRRLLWP IKKKYGNKIS WADLIALAGT IAYDVAGLKT FGFAFGREDI 

       190        200        210        220        230        240 
WAPEKDTYWG DEKEWLAPSD GRYGDVSKPE TLENPLAAVQ MGLIYVNPEG VNGKSDPLAT 

       250        260        270        280        290        300 
AAQMRETFAR MGMDDEETVA LTAGGHTIGK SHGNGSAANL SPDPEAAGPE YQGLGWINTK 

       310        320        330        340        350        360 
GRGIGRDTVV SGIEGAWTSE PTKWDNGFFD MLFKHEWTLT HSPAGASQWA PITIAEEDKP 

       370        380        390        400        410        420 
VDVEDASIRT IPMMTDADMA LKVDPIYREI SLKFKDDQDH FSDVFARAWF KLTHRDMGPK 

       430        440        450        460        470        480 
SRYVGPDVPA EDLIWQDPIP AGSTSYDVAA VKAKIAASGL SVADLVSTAW DSARTFRGSD 

       490        500        510        520        530        540 
KRGGANGARI RLAPQKDWEG NEPARLSRVL SVLEPIARET GASIADVIVL AGNYGVEQAA 

       550        560        570        580        590        600 
KAAGFDIAVP FAAGRGDASA EQTDADSFAP LEPLADGFRN WVKKDYVVSP EELLLDRAQL 

       610        620        630        640        650        660 
LGLTAPELTV LIGGLRVIGA NYGGAAHGVF TDKPGALTTD FFTTLTDMAY SWVPTGNNLY 

       670        680        690        700        710        720 
EIRDRKTGAA RYSATRVDLV IGSNSILRAY AEVYAQDDNR EKFARDFIAA WTKVMNADRF 


DLI

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References

[1]	"An Agrobacterium catalase is a virulence factor involved in tumorigenesis." Xu X.Q., Pan S.Q. Mol. Microbiol. 35:407-414(2000) [PubMed: 10652101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: A348.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB033631 Genomic DNA. Translation: BAA89349.1.
3D structure databases
HSSP	HSSP built from PDB template 1U2L based on UniProtKB P13029.
ProteinModelPortal	Q9R708.
SMR	Q9R708. Positions 24-722.
ModBase	Search...
Protein family/group databases
PeroxiBase	2692. AtuCP01_C58.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_01961. Catal-peroxid. [Tree]
InterPro	IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. [Graphical view]
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 2 hits.
TIGRFAMs	TIGR00198. Cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. False negative. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_RHIRD

Accession

Primary (citable) accession number: Q9R708

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	May 1, 2000
Last modified:	October 19, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families